scholarly journals Cooperative behavior of Escherichia coli cell-division protein FtsZ assembly involves the preferential cyclization of long single-stranded fibrils

2005 ◽  
Vol 102 (6) ◽  
pp. 1895-1900 ◽  
Author(s):  
J. M. Gonzalez ◽  
M. Velez ◽  
M. Jimenez ◽  
C. Alfonso ◽  
P. Schuck ◽  
...  
Keyword(s):  
Escherichia Coli ◽  
Cell Division ◽  
Cooperative Behavior ◽  
Coli Cell ◽  
Cell Division Protein ◽  
Ftsz Assembly

scholarly journals Phenylpropanoids inhibit protofilament formation of Escherichia coli cell division protein FtsZ

2011 ◽  
Vol 60 (9) ◽  
pp. 1317-1325 ◽  
Author(s):  
Shanmugam Hemaiswarya ◽  
Rohini Soudaminikkutty ◽  
Mohana Lakshmi Narasumani ◽  
Mukesh Doble
Keyword(s):  
Escherichia Coli ◽  
Cell Division ◽  
Coli Cell ◽  
Cell Division Protein

Berberine Targets Assembly of Escherichia coli Cell Division Protein FtsZ†

Biochemistry ◽  
2008 ◽  
Vol 47 (10) ◽  
pp. 3225-3234 ◽  
Author(s):  
Prerna N. Domadia ◽  
Anirban Bhunia ◽  
J. Sivaraman ◽  
Sanjay Swarup ◽  
Debjani Dasgupta
Keyword(s):  
Escherichia Coli ◽  
Cell Division ◽  
Coli Cell ◽  
Cell Division Protein

scholarly journals The Escherichia coli Cell Division Protein and Model Tat Substrate SufI (FtsP) Localizes to the Septal Ring and Has a Multicopper Oxidase-Like Structure

2009 ◽  
Vol 386 (2) ◽  
pp. 504-519 ◽  
Author(s):  
Michael Tarry ◽  
S.J. Ryan Arends ◽  
Pietro Roversi ◽  
Evan Piette ◽  
Frank Sargent ◽  
...  
Keyword(s):  
Escherichia Coli ◽  
Cell Division ◽  
Multicopper Oxidase ◽  
Coli Cell ◽  
Cell Division Protein

scholarly journals Activation of the Escherichia coli cell division protein FtsZ by a low-affinity interaction with monovalent cations

FEBS Letters ◽  
2006 ◽  
Vol 580 (20) ◽  
pp. 4941-4946 ◽  
Author(s):  
Michael Tadros ◽  
José Manuel González ◽  
Germán Rivas ◽  
Miguel Vicente ◽  
Jesús Mingorance
Keyword(s):  
Escherichia Coli ◽  
Cell Division ◽  
Coli Cell ◽  
Monovalent Cations ◽  
Cell Division Protein ◽  
Affinity Interaction

scholarly journals Epitope mapping of Escherichia coli cell division protein FtsZ with monoclonal antibodies.

1994 ◽  
Vol 176 (7) ◽  
pp. 1886-1893 ◽  
Author(s):  
J L Voskuil ◽  
C A Westerbeek ◽  
C Wu ◽  
A H Kolk ◽  
N Nanninga
Keyword(s):  
Escherichia Coli ◽  
Monoclonal Antibodies ◽  
Cell Division ◽  
Epitope Mapping ◽  
Coli Cell ◽  
Cell Division Protein

scholarly journals Localization of the Escherichia coli cell division protein FtsI (PBP3) to the division site and cell pole

1997 ◽  
Vol 25 (4) ◽  
pp. 671-681 ◽  
Author(s):  
David S. Weiss ◽  
Kit Pogliano ◽  
Michael Carson ◽  
Luz‐Maria Guzman ◽  
Claudine Fraipont ◽  
...  
Keyword(s):  
Escherichia Coli ◽  
Cell Division ◽  
Coli Cell ◽  
Cell Pole ◽  
Division Site ◽  
Cell Division Protein

scholarly journals Crystal structures of the cell-division protein FtsZ from Klebsiella pneumoniae and Escherichia coli

2020 ◽  
Vol 76 (2) ◽  
pp. 86-93
Author(s):  
Takuya Yoshizawa ◽  
Junso Fujita ◽  
Haruna Terakado ◽  
Mayuki Ozawa ◽  
Natsuko Kuroda ◽  
...  
Keyword(s):  
Escherichia Coli ◽  
Cell Division ◽  
Klebsiella Pneumoniae ◽  
Crystal Structures ◽  
Structural Basis ◽  
Bacterial Cell Division ◽  
Open Conformation ◽  
Cell Division Protein ◽  
Ftsz Assembly ◽  
Functional Analyses

FtsZ, a tubulin-like GTPase, is essential for bacterial cell division. In the presence of GTP, FtsZ polymerizes into filamentous structures, which are key to generating force in cell division. However, the structural basis for the molecular mechanism underlying FtsZ function remains to be elucidated. In this study, crystal structures of the enzymatic domains of FtsZ from Klebsiella pneumoniae (KpFtsZ) and Escherichia coli (EcFtsZ) were determined at 1.75 and 2.50 Å resolution, respectively. Both FtsZs form straight protofilaments in the crystals, and the two structures adopted relaxed (R) conformations. The T3 loop, which is involved in GTP/GDP binding and FtsZ assembly/disassembly, adopted a unique open conformation in KpFtsZ, while the T3 loop of EcFtsZ was partially disordered. The crystal structure of EcFtsZ can explain the results from previous functional analyses using EcFtsZ mutants.

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